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Entry: D0JB68_BLASB
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Original site: D0JB68_BLASB 
ID   D0JB68_BLASB            Unreviewed;       268 AA.
AC   D0JB68;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   13-SEP-2023, entry version 72.
DE   RecName: Full=Diaminopimelate epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE            Short=DAP epimerase {ECO:0000256|HAMAP-Rule:MF_00197};
DE            EC=5.1.1.7 {ECO:0000256|HAMAP-Rule:MF_00197};
DE   AltName: Full=PLP-independent amino acid racemase {ECO:0000256|HAMAP-Rule:MF_00197};
GN   Name=dapF {ECO:0000256|HAMAP-Rule:MF_00197,
GN   ECO:0000313|EMBL:ACY40406.1};
GN   OrderedLocusNames=BLBBGE_397 {ECO:0000313|EMBL:ACY40406.1};
OS   Blattabacterium sp. subsp. Blattella germanica (strain Bge) (Blattella
OS   germanica symbiotic bacterium).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=331104 {ECO:0000313|EMBL:ACY40406.1, ECO:0000313|Proteomes:UP000002625};
RN   [1] {ECO:0000313|EMBL:ACY40406.1, ECO:0000313|Proteomes:UP000002625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bge {ECO:0000313|Proteomes:UP000002625};
RX   PubMed=19911043; DOI=10.1371/journal.pgen.1000721;
RA   Lopez-Sanchez M.J., Neef A., Pereto J., Patino-Navarrete R., Pignatelli M.,
RA   Latorre A., Moya A.;
RT   "Evolutionary convergence and nitrogen metabolism in Blattabacterium strain
RT   Bge, primary endosymbiont of the cockroach Blattella germanica.";
RL   PLoS Genet. 5:E1000721-E1000721(2009).
CC   -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate
CC       (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-
CC       lysine and an essential component of the bacterial peptidoglycan.
CC       {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,6S)-2,6-diaminoheptanedioate = meso-2,6-
CC         diaminoheptanedioate; Xref=Rhea:RHEA:15393, ChEBI:CHEBI:57609,
CC         ChEBI:CHEBI:57791; EC=5.1.1.7; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00197};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- SIMILARITY: Belongs to the diaminopimelate epimerase family.
CC       {ECO:0000256|ARBA:ARBA00010219, ECO:0000256|HAMAP-Rule:MF_00197}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00197}.
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DR   EMBL; CP001487; ACY40406.1; -; Genomic_DNA.
DR   RefSeq; WP_012840921.1; NC_013454.1.
DR   AlphaFoldDB; D0JB68; -.
DR   STRING; 331104.BLBBGE_397; -.
DR   KEGG; bbl:BLBBGE_397; -.
DR   eggNOG; COG0253; Bacteria.
DR   HOGENOM; CLU_053306_3_2_10; -.
DR   OMA; HVAMRVH; -.
DR   OrthoDB; 9805408at2; -.
DR   UniPathway; UPA00034; UER00025.
DR   Proteomes; UP000002625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00197; DAP_epimerase; 1.
DR   InterPro; IPR001653; DAP_epimerase_DapF.
DR   NCBIfam; TIGR00652; DapF; 1.
DR   PANTHER; PTHR31689:SF0; DIAMINOPIMELATE EPIMERASE; 1.
DR   PANTHER; PTHR31689; DIAMINOPIMELATE EPIMERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01678; DAP_epimerase; 2.
DR   SUPFAM; SSF54506; Diaminopimelate epimerase-like; 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00197};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00197};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00197}.
FT   ACT_SITE        73
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   ACT_SITE        206
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         74..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         196..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   BINDING         207..208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            146
FT                   /note="Could be important to modulate the pK values of the
FT                   two catalytic cysteine residues"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
FT   SITE            196
FT                   /note="Could be important to modulate the pK values of the
FT                   two catalytic cysteine residues"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00197"
SQ   SEQUENCE   268 AA;  30775 MW;  E7489160451A38E3 CRC64;
     MKFNFFKYQG TGNDFILLDD RTKKIVKEYT ILKKLCNRHF GIGADGIILI QNDSKSDFYM
     QYYNSDGKES TMCGNGGRCA IFFAKKLGIN KENKIHFRAI DGHHYGLIIK NEKNDKCLVS
     INLINIQKNE IEIHPEHVFL NTGSPHHIIF VENIKEINVY EEGKKIRFRN PYLKKGVNVN
     FVEILENKTL QVRTYERGVE NETLSCGTGV TASVIAAYET NRISSIEKIL VHTIGGKLWV
     SLKETKNEYK DIYLTGSVQF IFQGCIFI
//
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